Genetic code expansion is a technology that allows for site-specific incorporation of noncanonical amino acids into recombinant proteins at amber stop codons using engineered translational machinery. The technology allows for expanded study into proteins, derived from the integration of novel chemical functions found in noncanonical amino acids, such as fluorescence,...
In biology, function and disease are closely intertwined, requiring the coordination of hundreds of intricate chemical reactions. Interdisciplinary cooperation between chemical and biological approaches is necessary to decipher the chemical links between physiological and pathological conditions. In this arena, the precision tools made possible with chemical biology can manipulate and...
Immobilized proteins are integral components of a number of important technologies, including the principal component of many biosensors, as functional coatings in various implants, as catalysts is industrial biosynthesis, and as the building blocks of next-generation nanotechnologies. Despite their ubiquity, relatively little is known about the processes that shape immobilized...
The buildup of reactive oxygen species (ROS) and reactive nitrogen and oxygen species (RNS) is known as oxidative stress. Oxidative stress results in a wide variety of modification to biological macromolecules including nucleic acids, lipids, and proteins. For at least 30 years it has been known that high levels of...
A specific tyrosine post-translational modification, called 3-nitro-tyrosine (nitroTyr), has been known to be present on an essential calcium signaling protein called calmodulin (CaM) during oxidative stress. While protein-bound 3-nitro-tyrosine has long been considered a biomarker of OS, it is also hypothesized to be a mechanism for protein signaling. However, purification...
Current protein immobilization techniques lack defined control over protein orientation. Protein orientation is important for making biosensors and biomaterials that are sensitive and efficient and can be crucial for designing some devices such as immunosensors or direct electron transferring biocells. A new method of protein immobilization is proposed that takes...
Current protein immobilization techniques lack defined control over protein orientation. Protein orientation is important for making biosensors and biomaterials that are sensitive and efficient and can be crucial for designing some devices such as immunosensors or direct electron transferring biocells. A new method of protein immobilization is proposed that takes...
This project deals with a method to optimize in vivo labeling using small fluorescent molecules via bioorthogonal reactions. The reaction used involves our unnatural amino acid 4-(6-methyl-s-tetrazin-3-yl)aminophenylalanine (AMT-Phe). The amino acid is site-specifically incorporated into GFP and then reacted with a labeled, strained trans-cyclooctene, resulting in a labeled protein. However...
This project deals with a method to optimize in vivo labeling using small fluorescent molecules via bioorthogonal reactions. The reaction used involves our unnatural amino acid 4-(6-methyl-s-tetrazin-3-yl)aminophenylalanine (AMT-Phe). The amino acid is site-specifically incorporated into GFP and then reacted with a labeled, strained trans-cyclooctene, resulting in a labeled protein. However...
The inverse electron demand Diels Alder reaction between tetrazines and strained alkenes is an exceptionally useful tool in functionalizing to biomolecules since it is orthogonal to the chemistry of most living systems and have exceptionally high rate constants. In particular reactions between strained trans-cyclooctenes (sTCO) and tetrazines can achieve second...